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Database: UniProt
Entry: A0A1T5FLE0_9MICC
LinkDB: A0A1T5FLE0_9MICC
Original site: A0A1T5FLE0_9MICC 
ID   A0A1T5FLE0_9MICC        Unreviewed;       417 AA.
AC   A0A1T5FLE0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Pyruvate dehydrogenase E1 component alpha subunit {ECO:0000313|EMBL:SKB96989.1};
GN   ORFNames=SAMN05660473_03364 {ECO:0000313|EMBL:SKB96989.1};
OS   Arthrobacter sp. 49Tsu3.1M3.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1279029 {ECO:0000313|EMBL:SKB96989.1, ECO:0000313|Proteomes:UP000189904};
RN   [1] {ECO:0000313|EMBL:SKB96989.1, ECO:0000313|Proteomes:UP000189904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=49Tsu3.1M3 {ECO:0000313|EMBL:SKB96989.1,
RC   ECO:0000313|Proteomes:UP000189904};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FUZD01000018; SKB96989.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5FLE0; -.
DR   Proteomes; UP000189904; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017596; PdhA/BkdA.
DR   InterPro; IPR029061; THDP-binding.
DR   NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR   PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:SKB96989.1}.
FT   DOMAIN          83..351
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   417 AA;  44629 MW;  0E979BDA668B3D6D CRC64;
     MTISADHAAQ PAAQQAAQQD PAGDAVSKFG ITVEDYMLPA RHQIQMVGPD GTLNPHTEQG
     TQPGHEYSLP SEAELMAAYE QLVIGRRVND QNSALVRQGR MAVYPSSHGQ EACQVAAALC
     LAEGDWLFPT YRDSVAVMAR GVDPVQTMTL FRGDWHGGYD PAKNKVGIQC TPLTTQLLHG
     VGVAHAAKLR GEDTVVLAMC GDGATSEGDF HEALNFAAVF HLPVVFFVQN NQYAISVPLA
     HQSVAPSLAH KAVGYGMAGE RVDGNDIVAL LAVLGRAVKL AREGSGPLLV EAHTYRMQAH
     TNADDATRYR QDSEVAEWVA KDPLSRMQTY LTDRGLLDDD RAAAIAEKAE AVATQLREGL
     SEEVPVEPQD LFKYVFSTPT PQLKEQSAML ADELARDAAS TATASAAATS ISREAGI
//
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